Electrostatic Complementarity Drives Amyloid/Nucleic Acid Co-Assembly.

ABSTRACT: Proteinaceous plaques associated with neurodegenerative diseases contain many biopolymers including the polyanions glycosaminoglycans and nucleic acids. Polyanion-induced amyloid fibrillation has been implicated in disease etiology, but structural models for amyloid/nucleic acid co-assemblies remain limited. Here we constrain nucleic acid/peptide interactions with model peptides that exploit electrostatic complementarity and define a novel amyloid/nucleic acid co-assembly. The structure provides a model for nucleic acid/amyloid co-assembly as well as insight into the energetic determinants involved in templating amyloid assembly.

SUBMITTER: Rha AK 

PROVIDER: S-EPMC6923580 | biostudies-literature | 2020 Jan

REPOSITORIES: biostudies-literature